Target intelligence / Profile preview

Sulfotransferase family 1C member 3 (SULT1C3)

Target
SULT1C3
Molecular classification
Enzyme, Cytosolic sulfotransferase
01

Overview

Sulfotransferase family 1C member 3 (SULT1C3) is a cytosolic enzyme that belongs to the broader family of sulfotransferases involved in the sulfate conjugation of a wide range of hormones, neurotransmitters, drugs, and xenobiotics. SULT1C3 exhibits marked substrate specificity, showing preference for relatively large and sometimes aromatic compounds, including environmental promutagens and procarcinogens. The enzyme facilitates detoxification and metabolic excretion but can also bioactivate certain compounds to potentially mutagenic or carcinogenic forms. SULT1C3 is primarily found in humans and other primates and is expressed in the cytoplasm of cells. Functional diversity exists due to alternative splicing, producing variants with different substrate specificities and catalytic efficiencies. Its physiological role remains incompletely understood, but aberrant function or expression may contribute to chemical-induced toxicity and possibly disease states, particularly those related to chemical carcinogenesis.

Other names
ST1C3Sulfotransferase 1C3
02

Mechanism of action

Catalyzes the transfer of a sulfo group from 3’-phosphoadenosine 5’-phosphosulfate (PAPS) to target molecules, typically hydroxyl groups of substrates, resulting in their sulfation

03

Biological functions

Sulfate conjugation of hormonesSulfate conjugation of neurotransmittersSulfate conjugation of drugsSulfate conjugation of xenobiotic compoundsMetabolism of xenobioticsMetabolism of cholesterol and bile acids
04

Disease associations

Cancer (due to activation of promutagens and procarcinogens)Other (potential roles in hormone and xenobiotic metabolism, significance in macular dystrophy based on gene-disease association, but not well-established mechanisms)
05

Safety considerations

Potential activation of procarcinogens, leading to mutagenic or carcinogenic metabolitesSubstrate specificity suggests risk in metabolic activation of environmental toxins in humans

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